ID A0A0G2EKX9_9EURO Unreviewed; 800 AA.
AC A0A0G2EKX9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
GN ORFNames=UCRPC4_g02937 {ECO:0000313|EMBL:KKY23422.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY23422.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY23422.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY23422.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY23422.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY23422.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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:KKY23422.1}.
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DR EMBL; LCWF01000068; KKY23422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2EKX9; -.
DR OrthoDB; 989271at2759; -.
DR Proteomes; UP000053317; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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:UP000053317}.
FT DOMAIN 150..523
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 569..695
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 733..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 87576 MW; BCCEDA445EC704C3 CRC64;
MTSPDVTLKV LSYALRGNKY KGKLLGTLNG IFQEALATSA PHLGLEAGSR VFSRLYVRFG
LTDTPTKMSG RFQLRRLYKP LAYAAAATAT SSIALYATSK PRGHNEPQAI PYTRDENGRI
IPPRFPSIKS RAEQIADLKC HSSTQDEIYD LLIIGGGATG TGIALDAATR GLRVALVERE
DFSSGTSSKS TKLVHGGVRY LEKAFWNLDY SQYQLVKEAL KERKNFLFTA PHLSSSLAIL
LPLYKWWEAP YFWAGTKAYD LLAGSEGLES SYFLTKNRAL EQFPLLKKDN LVGALVYYDG
QHNDSRMNVS LAMTAALYGA TMVNHIEVTG LEKDENGKLC GARVRDMLPE RDGQGKSSEQ
FIIRARGIIN ATGPFTDAIE QMDEPTRKDI VAPSSGVHIV LPGHLSPKNM GLLDPATSDG
RVIFFLPWEG STIAGTTDAP CGIERNPVAS EEDIGFILKE VNKYITPEID ITRDDVLAAW
SGIRPLVRDP NSANTESLVR NHLVTVSKSG LLTCAGGKWT TYRQMAEDAV DLAMSTFNLQ
PGPLPSSIRI GDQASSYSDI PTTARPGSCT TPSIRLLGSH GYSKTLYISL IQTFNLPADI
AQHLALNYGD RAWEVASLIS EVLSSSDHIP RLSRSHPFTP FEVLYSVRRE YAQTATDVLA
RRTRLSFLDA QAAYNALPTI IDIMGKELHW TQARKDMEFK LGVEFLGSMG LKDEFKLKQD
QNHELEHPQE NLFGHVSGLG SNARGPRFAG SPSHTGNTGT GAGTSGSKDG DRDRDRDYGF
RSPVGVSTGV FVAGSSRPEH
//
