ID A0A100IHE1_ASPNG Unreviewed; 704 AA.
AC A0A100IHE1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=ABL_04054 {ECO:0000313|EMBL:GAQ41295.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ41295.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ41295.1}.
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DR EMBL; BCMY01000006; GAQ41295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100IHE1; -.
DR PaxDb; 5061-CADANGAP00006217; -.
DR VEuPathDB; FungiDB:An08g00210; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1098376; -.
DR VEuPathDB; FungiDB:ATCC64974_106300; -.
DR VEuPathDB; FungiDB:M747DRAFT_150386; -.
DR OMA; WAMAPHI; -.
DR Proteomes; UP000068243; 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}; 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..456
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 502..629
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 675..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 77072 MW; AFAED6973AB856C8 CRC64;
MASRQSRRIL RPLLYTSLAA ATGAGVLYIS YRPRNIPGSE APAVPPPGYH EGKLVPPSFP
NIKSRLEQIQ DLKRSSGGSN SEEYDLLVIG GGATGSGIAL DAATRGLKVA IVERDDFSAG
TSSKSTKLVH GGVRYLEKAV WELDYNQYKL VKEALRERKY FLNTAPHLSS WLPIMVPLQK
WWQAPYFWAG TKFYDYLAGS EGIESSYFLT KSKAIDAFPM LRKDNLFGAM VYYDGAHNDS
RMNVSLAMTA ALYGATVVNH MQVTGLEKDS SGKLNGARVK DLIPGRDGQE AEEFTIKAKG
IINATGPFTD SIRQMDEPGI KEIVAPSSGV HVILPGYYSP SDMGLIDPST SDGRVIFFLP
WQGNTIAGTT DQPTEITPQP QPSEKDINWI ISEVRNYLAP DINIERSDVL AAWAGIRPLV
RDPKVKSSEA LVRNHLITVS PSGLLTCAGG KWTTYRQMAE EAVDEAIDVF GLKPRGVTGA
PDISGVGGSG LVSDGAVLDG SCQTHQVRLI GAHGFSKTLF INLIQHFGLE VDVAKHLTES
YGDRAWQVAA LSSPTNARFP VRGQRISRLY PFVDGEIRYA VRHEYAQTAT DVIARRTRLA
FLNAEAALEA LPNIIDLMGE ELKWDTNRKD SEWKESVQFL SSMGLPKAFL SMTREDVEAG
RVKDLDIAQR KAFARSDPPA DVLSSDIPSS DSNKLIHPES PANK
//