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Database: UniProt
Entry: A0A1Q3CAR1_CEPFO
LinkDB: A0A1Q3CAR1_CEPFO
Original site: A0A1Q3CAR1_CEPFO 
ID   A0A1Q3CAR1_CEPFO        Unreviewed;       628 AA.
AC   A0A1Q3CAR1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=CFOL_v3_20664 {ECO:0000313|EMBL:GAV77192.1};
OS   Cephalotus follicularis (Albany pitcher plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX   NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV77192.1, ECO:0000313|Proteomes:UP000187406};
RN   [1] {ECO:0000313|Proteomes:UP000187406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA   Fukushima K., Hasebe M., Fang X.;
RT   "Cephalotus genome sequencing.";
RL   Submitted (APR-2016) 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:GAV77192.1}.
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DR   EMBL; BDDD01001585; GAV77192.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3CAR1; -.
DR   STRING; 3775.A0A1Q3CAR1; -.
DR   InParanoid; A0A1Q3CAR1; -.
DR   OrthoDB; 989271at2759; -.
DR   Proteomes; UP000187406; 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; 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:UP000187406}.
FT   DOMAIN          74..442
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          464..599
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   628 AA;  68761 MW;  A89785206B8B851C CRC64;
     MSSAALRFRR LGYAAAAATT ASVFLAPSFS SNDRGGGSHL ESVRRGISDP NAVVPSRAVQ
     ESVLIGASSV NPLDVLVIGG GATGSGAALD AATRGLKVGL VEREDFSSGT SSRSTKLIHG
     GVRYLEKAVF NLDYGQLKLV FHALEERKQL IDNAPHLCHA LPCMTPCFDW FEVVYYWMGL
     KMYDLVAGRR LLHLSRYYSA QESAELFPTL AKKGHDRNLR GTVVYYDGQM NDSRLNVGLA
     CTAALAGAAI LNHAEAVSLL KDEATQRIIG ARIRDNISGK EFDTYAKVVV NAAGPFCDSV
     RKMVDKDTKS IICPSSGVHI VLPDYYSPEG MGLIVPKTKD GRVVFMLPWL GRTVAGTTDS
     DTVITLLPEP HEDEIQFILD AISDYLNVKV RRTDVLSAWS GIRPLAMDPK AKNTESISRD
     HVVFEDCPGL VTITGGKWTT YRSMAEDAVN AAIKYGKLSP RNDCITQSLR LVGGDGWEPS
     FFTILAQQYV RMKKTHDGKI VPGVMDTAAA KHLSHAYGTL AERVATIAQN EGLGKRLAHG
     YPYLEAEVAY CARYEYCESA VDFIARRSRL AFLDTNAAGR ALPRVIEILA TEHGWDKSRQ
     KQELQMGKDF LKTFKSSKNA QFHDGKHK
//
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