ID A0A0M9VN11_9BASI Unreviewed; 725 AA.
AC A0A0M9VN11;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=Malapachy_0539 {ECO:0000313|EMBL:KOS12859.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS12859.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS12859.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS12859.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-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:KOS12859.1}.
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DR EMBL; LGAV01000008; KOS12859.1; -; Genomic_DNA.
DR RefSeq; XP_017990491.1; XM_018135055.1.
DR AlphaFoldDB; A0A0M9VN11; -.
DR STRING; 77020.A0A0M9VN11; -.
DR GeneID; 28726930; -.
DR VEuPathDB; FungiDB:Malapachy_0539; -.
DR OrthoDB; 989271at2759; -.
DR Proteomes; UP000037751; 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: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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751}.
FT DOMAIN 128..498
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 520..647
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 687..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..725
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 79578 MW; 9DBDC5A7349F48DB CRC64;
MFRSAVRRLS QKAGVAANIN TPRGRAAVLA TAAVVSAGTV FALTRKGDWD DFAPSHDVSP
AQFWSPPTRS QMIEALKKSS RQGLRDDGSL EQKKSLLLPS HQAVGHSPIP EVEHAYVDRN
EDDDEGFDLL IVGGGATGAG CAVDAATRGL KVAIVERDDY GAGTSSKSTK LVHGGVRYLQ
KAVMQLDYEQ YKMVKEALHE RKTFLHIAPY LSNPLPILIP AYSWWLIPYY YAGTKLYDMI
AGRENMGNSY IVGREKALEL FPMLRSHNLA GGVVYYDGQQ NDTRMNIALI LTAIQHGAVA
ANHTEVVALN KAPSVNGQPG KIIGARLRDL LTGDEFDVKA KGVVNATGPF CDSLRKMDDP
SSPDIVAPSS GAHITFPGYF SPRGMGLLDP ATSDGRVIFF LPWQGSTIAG TTDTAAKVEA
HPLPGEQEIS WILDEVRNYL NADVTVKRTD VMSAWSGLRP LVKDPAARDT QSLVRNHMIN
VSDSGLLTIA GGKWTTYREM AEETINTAIK AYNLQPLRSC VSKQVRLIGS HSWSHTMYVR
LLQEFGLETE VAKHLSDSYG DRAWSVCAIA EHTGKRYPVH GVRLDSQLPY IEAEVRYATR
CEYATKAADF IARRSRMSFL NTEATIEALP RIIDIMGEEL DWSETRKQTE FQEGILFLSS
MGVEPSRVAE LAKHSLVEAR RWKDLSSPRQ VSPAMPNLTS GTPVPPVQTM PAANLPNLPN
IPPMP
//
