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Database: UniProt
Entry: A0A1B0BQW3_9MUSC
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ID   A0A1B0BQW3_9MUSC        Unreviewed;       680 AA.
AC   A0A1B0BQW3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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};
OS   Glossina palpalis gambiensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=67801 {ECO:0000313|EnsemblMetazoa:GPPI037768-PA, ECO:0000313|Proteomes:UP000092460};
RN   [1] {ECO:0000313|Proteomes:UP000092460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000092460};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GPPI037768-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPPI037768-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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; JXJN01018834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A1B0BQW3; -.
DR   STRING; 67801.A0A1B0BQW3; -.
DR   EnsemblMetazoa; GPPI037768-RA; GPPI037768-PA; GPPI037768.
DR   VEuPathDB; VectorBase:GPPI037768; -.
DR   Proteomes; UP000092460; 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: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; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 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}.
FT   DOMAIN          66..410
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          469..591
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   680 AA;  76323 MW;  6F73E333C16D2614 CRC64;
     MASFLYKLGV AALGTTVGSS LAGWTFDRWN PTRKVINPPS RLPIHRSHLI SRAMQIQNLQ
     RESEFDVLVI GGGSTGAGCA LDAVTRGLKT ALVEADDFAS GTSSKSASTK LMEDGAQCLQ
     KAMTESDYKK QCSIVKEVLR EKASLSESAP HLVHPLPIML PVYEWWQIPL YWVGTKCYDL
     AAGDRNVKGS YFLSKRDALE LFPTLKKDKL VGAIVYYDGQ DDDARMCLAV VVTAARHGAT
     VCNHVEVLKL LKKDDGKGGY VLYGVEVIDH MSGKKFIIKA KCVVNATGSF NNSIRKMDDP
     TISICDPSSC AHIVLPGYYS PEQMSLLDPF TSEDRVVFFL PWQMHTIDDT TDTPHIVKEK
     PAPSDEGVQY ILNEIQDYVN SDVDVRHDDV LSVWSDIPPS PTTPSVVSQP KKDDTQLWTH
     NHTIHISPSN LITVAGDKVT TSRARAERVI DTAVEVCNLK PWSKSIRNTL KIENGQNWSS
     TMYARLVQGY GLEYEVAQHL AKLYGDRAFE VAKMASLTGK RWPIAGNRIH PDFPCIDAEV
     RYGVREYACN AVDMIARRLR LSYLNVQAAQ ESLPRICDIM AEELNWSNEE KKKQIKKAKQ
     YLAFEMGQAT KRNRAKHQMY LNLSKEEKEL CAKRFERLDR DEKHSRGFKQ GFGDCDFSDD
     ILKDIDVNVI GDYLKIKRHC
//
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