GPDM_CAEEL
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 03-AUG-2022, entry version 157.
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}.
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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; 9.
DR STRING; 6239.T25G3.4; -.
DR EPD; P90795; -.
DR PaxDb; P90795; -.
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 CTD; 172509; -.
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; CIVNAAG; -.
DR OrthoDB; 669193at2759; -.
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 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:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase 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; -; 1.
DR Gene3D; 3.50.50.60; -; 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; PTHR11985; 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; SSF47473; 1.
DR SUPFAM; SSF51905; SSF51905; 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