ID A0A212F3S6_DANPL Unreviewed; 753 AA.
AC A0A212F3S6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=KGM_201301 {ECO:0000313|EMBL:OWR48372.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR48372.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR48372.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR48372.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
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 -!- PATHWAY: Polyol metabolism; glycerol degradation.
CC {ECO:0000256|ARBA:ARBA00004745}.
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:OWR48372.1}.
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DR EMBL; AGBW02010507; OWR48372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212F3S6; -.
DR STRING; 278856.A0A212F3S6; -.
DR KEGG; dpl:KGM_201301; -.
DR eggNOG; KOG0042; Eukaryota.
DR InParanoid; A0A212F3S6; -.
DR Proteomes; UP000007151; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 CDD; cd00051; EFh; 1.
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; 1.10.238.10; EF-hand; 2.
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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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 Pfam; PF13499; EF-hand_7; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 613..648
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 682..717
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 753 AA; 84045 MW; EF9A0B24ED32AFC6 CRC64;
MSRRKLVVCG AGAAGAVVAA WALSADDRLG SWYKSTTVAA KSERRKRPLP SRTDQIKNLQ
AGHTYDVLII GGGATGAGCA LDATTRGLRT ALVEADDFAS GTSSRSTKLI HGGVRYLQKA
IMQLDYEQYK MVKEALHERA NMLEVAPHLT RPLPILLPVY KWWQVPYYWF GIKMYDLVAG
DRNLKSSYYL SKKNTLELFP MLKSDNLCGG IVYYDGQQDD ARMNLAIALT AARHGATITN
HVSVVKLHKT DGKLSGARVR DELTGKEWDV KAKSIINATG PFTDSIRKMD DQTIKDICCP
SSGVHIVLPG YYSPEHMGLL DPATSDGRVI FFLPWLKGTI AGTTDMPCQV THNPKPTEDE
ILFILTEVKN YLNPDVEVRR GDVLSAWSGI RPLVSDPNKP DTQSLARNHI VHVSPSGLVT
IAGGKWTTYR AMAAEAVDAA IESCNLKPLY KECQTDGFLI EGAHGWTPTM YIRLVQDFGL
EMEVAQHLAK SYGDRAFAVA KMAAMTGKRW PIIGKKIHPE FPYIDAEIRY GVREYACTAV
DMIARRLRLA FLNVQAAAEA LPAVIEIMAE ELKWNEAERQ KQTKIAADFL ANEMGQMVNR
ASRDKIPINL NKEEIQTYIK RFQIIDKDRK GFVSINDIRR SLKSMGVKPS DDEISAILSE
IDVTYHGQLE IQDYLQNYGE DVTGEQLHEI LREIDTNMNG QVELDEYLQM MSAIKSGHVA
YSRFARMAEL EEEHHEKETL KKKITVERSG GGL
//
