ID A0A2S6GX32_9PSEU Unreviewed; 579 AA.
AC A0A2S6GX32;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=CLV40_103367 {ECO:0000313|EMBL:PPK69757.1};
OS Actinokineospora auranticolor.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=155976 {ECO:0000313|EMBL:PPK69757.1, ECO:0000313|Proteomes:UP000239203};
RN [1] {ECO:0000313|EMBL:PPK69757.1, ECO:0000313|Proteomes:UP000239203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YU 961-1 {ECO:0000313|EMBL:PPK69757.1,
RC ECO:0000313|Proteomes:UP000239203};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (FEB-2018) 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:PPK69757.1}.
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DR EMBL; PTIX01000003; PPK69757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6GX32; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000239203; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000239203}.
FT DOMAIN 35..383
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 411..533
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 579 AA; 62841 MW; EE19FD98D539C4B8 CRC64;
MASRTPHSTS DSPGGVLGPA ERDRAWRRLA AEPFDVVVIG GGIVGCGVAL DAATRGLRVA
LVEARDLASG TSSRSSKLFH GGLRYLEQLE FGLVREALRE RELMLTRIAP HLVKPVSFLY
PLRHRGWERP YTAAGLFLYD TMGGARSVPG QKHLTRAGAL RMVPALRRDA LIGGIRYYDA
QADDARHTMT VARTAAHYGA VVRASTQVVG FTREADRVSG VRVRDVETGA ETVVRADVVV
NCTGVWTDEL QRASGSRGRF RVRASKGVHI VVARDRIVAE SGLILRTAKS VLFVIPWRNH
WIVGTTDTDW NLDLAHPAAT RQDIDYILAQ VNSVLATPLT HDDIEGVYAG LRPLLAGESE
ETSKLSREHA VARVAPGLVA IAGGKYTTYR VMAADAVDAA AVDLPGRLRP SITDQVPLLG
ADGYHALVNQ ADLLAARYGL HPYRVRHLLD RYGSLVHAVL ELATPELLKP VDAAPDYLLV
EIAYAAAAEG ALHVEDVLTR RTRISMEYAH RGVDCARQVA EVMAGVLGWD EDRVEFEIAN
YVARVAAERD SQIKPDDAAA DAVRAGAPDV REFLVSPVS
//
