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Database: UniProt
Entry: A0A100IHE1_ASPNG
LinkDB: A0A100IHE1_ASPNG
Original site: A0A100IHE1_ASPNG 
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
//
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