ID A0A0G2H4C9_9PEZI Unreviewed; 687 AA.
AC A0A0G2H4C9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=UCDDA912_g09974 {ECO:0000313|EMBL:KKY30098.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY30098.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY30098.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY30098.1};
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:KKY30098.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY30098.1};
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:KKY30098.1}.
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DR EMBL; LCUC01000534; KKY30098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2H4C9; -.
DR STRING; 1214573.A0A0G2H4C9; -.
DR OrthoDB; 989271at2759; -.
DR Proteomes; UP000034680; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..463
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 506..632
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 687 AA; 75933 MW; 5166994110D32081 CRC64;
MSGFTRARPG LLRRLVLPVG LATAGGGLLF YVYRPRNIPG HGAAAVPPPI YGADGTFKLP
KFPRVMSRSE QIADLKKSAS AAADKSDEYE YDMLVIGGGA TGAGVAVDAA TRGLRVAVVE
RDDFSSGTSS KSTKLVHGGV RYLEKAVWNL DYNQYQLVRE ALKERKYFLQ TAPHLSSWLP
IMLPLDKWWK APYYWAGTKF YDFLAGSEGI ESSYFLTKSK AIEAFPMLKR TDLVGALVYY
DGAHNDSRMN VSIAMTAALY GATVVNHIEV TGLDKDANGK LSGARLKDLV PERDGKAADE
FHVKAKCIIN CTGPFADGIR KLDEQDCKEI VAPASGVHVI LPGYYSPAKM GLIDPSTSDG
RVIFFLPWQG NTIAGTTDKP AKVTKDPMPD EESIQWILKE VSNYLSPDIV VRRGDVLAAW
SGLRPLVKDP KAKNTESLVR NHLIDISESG LVTCAGGKWT TYRQMAEECV DAAVREFGLQ
TRPVPDAPRV SGTDAIDDGA ILDGSCQSHR VRLIGAHGWS RTLFINLIQH YGVETEVAKH
LCENYGDRAW VVAALCRATD KRFPARGERV SQLYPFVDGE IRYAVRHEYA QTAVDVLARR
TRLAFLNAQA ALECLPQVID IMASELSWDK RRQEVEWRDT VAFLESMGLP KPMLSATRSQ
VEQGKLDFRT GLEYKMYSRH DKPADEE
//
