ID   GPDM_DICDI              Reviewed;         638 AA.
AC   Q54QC1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
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   ORFNames=DDB_G0283951;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- 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; AAFI02000058; EAL65463.1; -; Genomic_DNA.
DR   RefSeq; XP_638823.1; XM_633731.1.
DR   AlphaFoldDB; Q54QC1; -.
DR   SMR; Q54QC1; -.
DR   STRING; 44689.Q54QC1; -.
DR   PaxDb; 44689-DDB0185769; -.
DR   EnsemblProtists; EAL65463; EAL65463; DDB_G0283951.
DR   GeneID; 8624347; -.
DR   KEGG; ddi:DDB_G0283951; -.
DR   dictyBase; DDB_G0283951; -.
DR   eggNOG; KOG0042; Eukaryota.
DR   HOGENOM; CLU_015740_4_1_1; -.
DR   InParanoid; Q54QC1; -.
DR   OMA; PHIVKPM; -.
DR   PhylomeDB; Q54QC1; -.
DR   Reactome; R-DDI-1483166; Synthesis of PA.
DR   Reactome; R-DDI-163560; Triglyceride catabolism.
DR   UniPathway; UPA00618; UER00673.
DR   PRO; PR:Q54QC1; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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   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; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..638
FT                   /note="Probable glycerol-3-phosphate dehydrogenase,
FT                   mitochondrial"
FT                   /id="PRO_0000355967"
FT   BINDING         100..128
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   638 AA;  71425 MW;  19DA700617840BBC CRC64;
     MNQLLSKSFK PLVVAGVAVI GISAFSGNRA YDEYRKERES ISKKMINDLN ENKITMFDYF
     QECKTLGRDE QLSKLNKLSK VYNKQKLNEQ ENQEELIDLD LIVIGGGATG TGVALDAQSR
     GMKVALFEKY DFSSGTSSKS TKLVHGGIRY LESAIMKLKP SELTLVKEAL RERSNLLNNA
     PHLSRQLPIV IPAYSIFDAS KFWIGCKLYD FFYPFNDIPK SYLQTSAQTY KEFPFLREGL
     VSSVVYYDGQ HNDSRMNVSL ALTAAQQGAL TLNYTEVVEL IKDDKINNNN KQQQLKGVVI
     RDRLTGKKYS VPAKCVVNAT GPYCDSIRNL DDPRADPIIT ASSGVHIMLP GNLIPSDKGF
     LNPKTKDGRV LFILPFEGKT LVGTTDDPSP IIENPQPLEK DVEFILDSIK EYSNPNVKLD
     KSQVLACWSG IRPLVSDEPA AQGDNKKSTS QVTRSHSLRM SESGLITIVG GKWTTYRSMA
     EATVNLVCSK HDIFTPKGCI TKNLPLIGGE KYYNTLNQYL IKNFNLPEDI AEHLAHSYGD
     QAPFVAKLAN ENGSNKRLVE GYPYIEAEVT YGVKKEYACT AEDIIGRRTR LSFLDHDKAE
     IALPKIINIM APLLKWSNER KKEELKNSQN YLKTMTSK
//