ID A0A0C3CAA0_HEBCY Unreviewed; 777 AA.
AC A0A0C3CAA0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=M413DRAFT_445847 {ECO:0000313|EMBL:KIM41129.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM41129.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM41129.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-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}.
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DR EMBL; KN831781; KIM41129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3CAA0; -.
DR STRING; 686832.A0A0C3CAA0; -.
DR HOGENOM; CLU_015740_3_1_1; -.
DR OrthoDB; 989271at2759; -.
DR Proteomes; UP000053424; 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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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:UP000053424};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..450
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 474..600
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 777 AA; 85164 MW; AB2A6E7A3E522FA1 CRC64;
MAILSRVFSR RTLACAAGGT TVFVAGGYWY LNSGPSYPAP VMATRRPPPP WTPPSRSEML
NRLKASGTIT KLAKGAQTSE GEEFDLLIIG GGATGAGCAV DAASRGLKVA LVERDDFSAG
TSSKSTKLVH GGVRYLQKAV MELDYDQYKL VREALHERRI FLQTAPYLSQ MLPIMLPIYK
YWQVPYYWAG CKMYDVLAGK ENMETSYLMS KGKALETFPM LKSDGLVGAL VYYDGQHNDS
RTNMALIMSA VKHGATVANY CEVTQLHKDT NGNLNGAKVK DNLTGEEWDV RAKGIVNATG
PFSDAMLSLD NPSHEAIVQP SSGVHITLPN YYSPRKMGLL DPATSDGRVI FFLPWQGNTI
AGTTDTRANV SRDPVASEED IRWLLEEVRR YLSPDIKVRR GDVLSAWSGL RPLVRDPNAE
KTEGLVRNHM INVSESGLLT IAGGKWTTYR AMAEETIDKA VEVFGFQERV RNGCVTESLR
LVGSDGWSRN MFIGLIQTYG LETDVAKHLS ENYGDRAWTV CSLAQPTGKA WPLHGERLAP
QYPFIDAEVR YAIRNEYAVS AIDVLARRTR LSFLNARAAL DALPRVVEIM ADELQWSYAE
RQRQIANTVR FLESMGLNAP SSITPAPIPR GFVEKASEAV KRAGSWALGY GRGADVTIES
FGPGRSRFEA GEVAALRTAF GGKAKVSVPG GGDGDVAELK VRMDEVMDIL RSVPGYPEIS
KKELDYVVAE AGMDGQKDVD LDEFIELSGS LKEVLFAPVI EKKARRKIPV EKSGGGV
//
