ID   GPDM_CAEEL              Reviewed;         722 AA.
AC   P90795; Q22793;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Probable glycerol-3-phosphate dehydrogenase, mitochondrial;
DE            Short=GPD-M;
DE            Short=GPDH-M;
DE            EC=1.1.5.3;
DE   Flags: Precursor;
GN   Name=gpdh-3 {ECO:0000312|WormBase:T25G3.4};
GN   ORFNames=T25G3.4 {ECO:0000312|WormBase:T25G3.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Calcium-binding enhances the activity of the
CC       enzyme. {ECO:0000250}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX284601; CAA96690.1; -; Genomic_DNA.
DR   EMBL; Z73906; CAA96690.1; JOINED; Genomic_DNA.
DR   PIR; T20362; T20362.
DR   RefSeq; NP_492115.1; NM_059714.4.
DR   AlphaFoldDB; P90795; -.
DR   SMR; P90795; -.
DR   BioGRID; 37951; 10.
DR   STRING; 6239.T25G3.4.1; -.
DR   EPD; P90795; -.
DR   PaxDb; 6239-T25G3-4; -.
DR   PeptideAtlas; P90795; -.
DR   EnsemblMetazoa; T25G3.4.1; T25G3.4.1; WBGene00012031.
DR   GeneID; 172509; -.
DR   KEGG; cel:CELE_T25G3.4; -.
DR   UCSC; T25G3.4; c. elegans.
DR   AGR; WB:WBGene00012031; -.
DR   WormBase; T25G3.4; CE14180; WBGene00012031; gpdh-3.
DR   eggNOG; KOG0042; Eukaryota.
DR   GeneTree; ENSGT00390000001718; -.
DR   HOGENOM; CLU_015740_3_1_1; -.
DR   InParanoid; P90795; -.
DR   OMA; PHIVKPM; -.
DR   OrthoDB; 989271at2759; -.
DR   PhylomeDB; P90795; -.
DR   Reactome; R-CEL-1483166; Synthesis of PA.
DR   Reactome; R-CEL-163560; Triglyceride catabolism.
DR   UniPathway; UPA00618; UER00673.
DR   PRO; PR:P90795; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00012031; Expressed in adult organism and 4 other cell types or tissues.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; 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; 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; FAD; Flavoprotein; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..43
FT                   /note="Mitochondrion"
FT   CHAIN           44..722
FT                   /note="Probable glycerol-3-phosphate dehydrogenase,
FT                   mitochondrial"
FT                   /id="PRO_0000010432"
FT   DOMAIN          624..659
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          660..695
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         76..104
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         673
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         675
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         677
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         679
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         684
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   722 AA;  80807 MW;  9E8BF74246480E30 CRC64;
     MSWVRFTKTG VAVVATSAAA VLALDMTNER RFQRQVKDHF RTVHADRLAE LNKRAPSALP
     TRKDILTNLS KGEEFDVLII GGGATGAGVA LDAQTRGLKT ALVELDDFSS GTSSRSTKLI
     HGGVRYLQAA IMKLDLEQYR MVKEALFERH NLLEIAPHLS SPLPIMLPIY KLWQVPYYWS
     GIKAYDFVSG KRVLKNSFFI NKSQALERFP MLRNESLKGA LIYYDGQHND ARMNLAIILT
     AIRHGAACAN HVRVEKLNKD ETGKVIGAHV RDMVTGGEWD IKAKAVINAT GPFTDSIRLM
     GDPETARPIC APSSGVHITL PGYYSPSNTG LLDPDTSDGR VIFFLPWERM TIAGTTDAPS
     DVTLSPQPTD HDIEFILQEI RGYLSKDVSV RRGDVMSAWS GLRPLVRDPN KKDTKSLARN
     HIIEVGKSGL ITIAGGKWTT YRHMAEETVD RVVEVHGLKT ENGCVTPGLL LEGAHDWNSL
     QYIHLVQDYG MEVDVAQHLS NTYGDRAFVV ARMCKMTGKR WPIVGQRLHP EFPYLDAEVR
     YAVREYACTA IDVIARRMRL AFLNTYAAHE VLPDVVRVMG QELGWSSAEQ RAQLEKARTF
     IDMEMGQNAK QTAVSNVALN LTKEEMQRAK ERFQQLDKDR KGHITVNDLR KHFREHNQKI
     DERVLHELLN EVDLNKNGEI EIAEFFQLYS GLKGGQLTGN RLVGYLDEIH GTPSVNRACG
     GI
//