ID A0A229TDJ5_9PSEU Unreviewed; 562 AA.
AC A0A229TDJ5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=CF165_10920 {ECO:0000313|EMBL:OXM69193.1};
OS Amycolatopsis vastitatis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1905142 {ECO:0000313|EMBL:OXM69193.1, ECO:0000313|Proteomes:UP000215199};
RN [1] {ECO:0000313|Proteomes:UP000215199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H5 {ECO:0000313|Proteomes:UP000215199};
RA Adamek M., Alanjary M., Sales-Ortells H., Goodfellow M., Bull A.T.,
RA Kalinowski J., Ziemert N.;
RT "Comparative genome mining reveals phylogenetic distribution patterns of
RT secondary metabolites in Amycolatopsis.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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:OXM69193.1}.
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DR EMBL; NMUL01000008; OXM69193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229TDJ5; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000215199; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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; PS00977; FAD_G3PDH_1; 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 ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 22..376
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 399..522
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 539..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 61121 MW; 5743C02EDDBC7B84 CRC64;
MTPLSPQYRA ETLRKLVNEE VDVLVVGGGV TGAGVALDAA SRGLSTALVE ARDFAAGTSS
RSSKLIHGGL RYLEQLDFKL VREALKERGL LLQKLAPHLV RPVKFLVPLT HRVWERGYIG
AGVTLYDTLG GARALPRHRH LSKRGAFKAA PALADDALIG AIQYYDAQVD DARHTMTIAR
TAAEQGASVL TRARVTSLLR DGERVVGAKV VDRESGIEFE IRARTVVAAT GVWSDDMAEA
AGIPAPFTVR ASKGIHLVVP REKIDLDTGL ILRTEKSVLF VIPWGRHWIV GTTDTEWDLD
REHPAASRAD VDYVLEHLNA VLRTPVTHDD IEGVYAGLRP LLAAKAAATT KLSREHAVAH
PVPGLVIVAG GKYTTYRVMA ADAVDVAVEE IGRPAPPSWT DRLPIVGAEG YHELWEDRFA
VAAKSGLPLT RVEHLLQRYG TRIWNLLDLV EQDRELGAPI TETSEYLRAE AVYAVSHEGA
LHLEDVLTRR TRISIEERDR GVAAAPVVAA LMAPLLGWDA HKEEREVANY LARVEAERSA
QEAPDDAAAN ATRLAAPALL PS
//
